{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T05:06:11Z","timestamp":1777525571193,"version":"3.51.4"},"reference-count":67,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T00:00:00Z","timestamp":1669852800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2022,12]]},"DOI":"10.1016\/j.bioorg.2022.106204","type":"journal-article","created":{"date-parts":[[2022,10,13]],"date-time":"2022-10-13T13:28:27Z","timestamp":1665667707000},"page":"106204","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Peptide inhibitors of angiotensin-I converting enzyme based on angiotensin (1\u20137) with selectivity for the C-terminal domain"],"prefix":"10.1016","volume":"129","author":[{"given":"Rogerio L.","family":"da Silva","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Athanasios","family":"Papakyriakou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adriana K.","family":"Carmona","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Georgios A.","family":"Spyroulias","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edward D.","family":"Sturrock","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9262-2151","authenticated-orcid":false,"given":"Patr\u00edcia A.","family":"Bersanetti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clovis R.","family":"Nakaie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.bioorg.2022.106204_b0005","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1084\/jem.103.3.295","article-title":"The preparation and function of the hypertensin-converting enzyme","volume":"103","author":"Skeggs","year":"1956","journal-title":"J. Exp. Med."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0010","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/0005-2795(70)90017-6","article-title":"A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin","volume":"214","author":"Yang","year":"1970","journal-title":"Biochim. Biophys. Acta"},{"issue":"5117","key":"10.1016\/j.bioorg.2022.106204_b0015","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1038\/216762a0","article-title":"Conversion of angiotensin I to angiotensin II","volume":"216","author":"Ng","year":"1967","journal-title":"Nature."},{"issue":"9","key":"10.1016\/j.bioorg.2022.106204_b0020","doi-asserted-by":"crossref","first-page":"5540","DOI":"10.1016\/S0021-9258(19)67628-3","article-title":"Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes","volume":"266","author":"Wei","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0025","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1016\/S0021-9258(17)40657-0","article-title":"Serum angiotensin-converting enzyme. Isolation and relationship to the pulmonary enzyme","volume":"252","author":"Das","year":"1977","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2022.106204_b0030","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1152\/physrev.00036.2005","article-title":"Physiology of local renin-angiotensin systems","volume":"86","author":"Paul","year":"2006","journal-title":"Physiol. Rev."},{"issue":"14","key":"10.1016\/j.bioorg.2022.106204_b0035","doi-asserted-by":"crossref","first-page":"9002","DOI":"10.1016\/S0021-9258(18)31543-6","article-title":"The two homologous domains of human angiotensin I-converting enzyme are both catalytically active","volume":"266","author":"Wei","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"24","key":"10.1016\/j.bioorg.2022.106204_b0040","doi-asserted-by":"crossref","first-page":"9386","DOI":"10.1073\/pnas.85.24.9386","article-title":"Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning","volume":"85","author":"Soubrier","year":"1988","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1\u20132","key":"10.1016\/j.bioorg.2022.106204_b0045","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0014-5793(89)80897-X","article-title":"The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme","volume":"252","author":"Lattion","year":"1989","journal-title":"FEBS Lett."},{"issue":"11","key":"10.1016\/j.bioorg.2022.106204_b0050","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1038\/nm1105-1140","article-title":"Male fertility is dependent on dipeptidase activity of testis ACE","volume":"11","author":"Fuchs","year":"2005","journal-title":"Nat. Med."},{"issue":"16","key":"10.1016\/j.bioorg.2022.106204_b0055","doi-asserted-by":"crossref","first-page":"7807","DOI":"10.1073\/pnas.91.16.7807","article-title":"Naturally occurring active N-domain of human angiotensin I-converting enzyme","volume":"91","author":"Deddish","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"13","key":"10.1016\/j.bioorg.2022.106204_b0060","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1016\/S0021-9258(18)98378-X","article-title":"Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides","volume":"268","author":"Jaspard","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0065","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1161\/HYPERTENSIONAHA.107.097865","article-title":"Angiotensin-converting enzyme C-terminal catalytic domain is the main site of angiotensin I cleavage in vivo","volume":"51","author":"Fuchs","year":"2008","journal-title":"Hypertension."},{"issue":"8","key":"10.1016\/j.bioorg.2022.106204_b0070","doi-asserted-by":"crossref","first-page":"3656","DOI":"10.1074\/jbc.270.8.3656","article-title":"The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin- converting enzyme","volume":"270","author":"Rousseau","year":"1995","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2022.106204_b0075","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1124\/pr.112.006809","article-title":"A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme","volume":"65","author":"Bernstein","year":"2013","journal-title":"Pharmacol. Rev."},{"issue":"4288","key":"10.1016\/j.bioorg.2022.106204_b0080","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1126\/science.191908","article-title":"Design of specific inhibitors of angiotensin-converting enzyme: new class of orally active antihypertensive agents","volume":"196","author":"Ondetti","year":"1977","journal-title":"Science."},{"issue":"9","key":"10.1016\/j.bioorg.2022.106204_b0085","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1111\/j.1751-7176.2011.00508.x","article-title":"Angiotensin-converting enzyme inhibitors","volume":"13","author":"Izzo","year":"2011","journal-title":"J. Clin. Hypertens."},{"issue":"11","key":"10.1016\/j.bioorg.2022.106204_b0090","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/nrd1227","article-title":"ACE revisited: a new target for structure-based drug design","volume":"2","author":"Acharya","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"issue":"3","key":"10.1016\/j.bioorg.2022.106204_b0095","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1172\/JCI118484","article-title":"Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline","volume":"97","author":"Azizi","year":"1996","journal-title":"J. Clin. Invest."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0100","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/S0022-3565(24)29576-8","article-title":"RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis","volume":"297","author":"Junot","year":"2001","journal-title":"J. Pharmacol. Exp. Ther."},{"issue":"6","key":"10.1016\/j.bioorg.2022.106204_b0105","doi-asserted-by":"crossref","first-page":"845","DOI":"10.2174\/092986712799034950","article-title":"Structure based drug design of angiotensin-I converting enzyme inhibitors","volume":"19","author":"Anthony","year":"2012","journal-title":"Curr. Med. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2022.106204_b0110","doi-asserted-by":"crossref","first-page":"4330","DOI":"10.1073\/pnas.96.8.4330","article-title":"RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites","volume":"96","author":"Dive","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0115","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1161\/01.RES.0000081593.33848.FC","article-title":"Roles of the two active sites of somatic angiotensin-converting enzyme in the cleavage of angiotensin I and bradykinin insights from selective inhibitors","volume":"93","author":"Georgiadis","year":"2003","journal-title":"Circ. Res."},{"issue":"25","key":"10.1016\/j.bioorg.2022.106204_b0120","doi-asserted-by":"crossref","first-page":"8048","DOI":"10.1021\/bi049504q","article-title":"Structural determinants of RXPA380, a potent and highly selective inhibitor of the angiotensin-converting enzyme C-domain","volume":"43","author":"Georgiadis","year":"2004","journal-title":"Biochemistry."},{"issue":"5","key":"10.1016\/j.bioorg.2022.106204_b0125","doi-asserted-by":"crossref","first-page":"E1","DOI":"10.1161\/01.RES.87.5.e1","article-title":"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1\u20139","volume":"87","author":"Donoghue","year":"2000","journal-title":"Circ. Res."},{"issue":"43","key":"10.1016\/j.bioorg.2022.106204_b0130","doi-asserted-by":"crossref","first-page":"33238","DOI":"10.1074\/jbc.M002615200","article-title":"A human homolog of angiotensin-converting enzyme: cloning and functional expression as a captopril-insensitive carboxypeptidase","volume":"275","author":"Tipnis","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2022.106204_b0135","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1152\/physrev.00023.2016","article-title":"The ACE2\/angiotensin-(1\u20137)\/mas axis of the renin-angiotensin system: focus on angiotensin-(1\u20137)","volume":"98","author":"Santos","year":"2018","journal-title":"Physiol. Rev."},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0140","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1161\/01.HYP.31.4.912","article-title":"N-domain-specific substrate and c-domain inhibitors of angiotensin- converting enzyme angiotensin-(1\u20137) and keto-ace","volume":"31","author":"Deddish","year":"1998","journal-title":"Hypertension."},{"issue":"6","key":"10.1016\/j.bioorg.2022.106204_b0145","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1097\/00004872-199606000-00017","article-title":"Effects of captopril related to increased levels of prostacyclin and angiotensin-(1\u20137) in essential hypertension","volume":"14","author":"Luque","year":"1996","journal-title":"J. Hypertens."},{"issue":"18","key":"10.1016\/j.bioorg.2022.106204_b0150","doi-asserted-by":"crossref","first-page":"5473","DOI":"10.1021\/bi700275e","article-title":"The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380","volume":"46","author":"Corradi","year":"2007","journal-title":"Biochemistry."},{"issue":"10","key":"10.1016\/j.bioorg.2022.106204_b0155","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1042\/BCJ20190290","article-title":"Structural basis for the C-domain-selective angiotensin-converting enzyme inhibition by bradykinin-potentiating peptide b (BPPb)","volume":"476","author":"Sturrock","year":"2019","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0160","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of the active site in proteases. I. Papain","volume":"27","author":"Schechter","year":"1967","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0165","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/s00726-018-2662-z","article-title":"Fragments of the second transmembrane helix of three G-protein-coupled receptors: comparative synthetic, structural and conformational studies","volume":"51","author":"Lopes","year":"2019","journal-title":"Amino Acids"},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0170","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/0003-2697(70)90146-6","article-title":"Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides","volume":"34","author":"Kaiser","year":"1970","journal-title":"Anal. Biochem."},{"issue":"9","key":"10.1016\/j.bioorg.2022.106204_b0175","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1248\/cpb.49.1089","article-title":"Evaluation of the trifluoromethanosulfonic acid\/trifluoroacetic acid\/thioanisole cleavage procedure for application in solid-phase peptide synthesis","volume":"49","author":"Jubilut","year":"2001","journal-title":"Chem. Pharm. Bull."},{"issue":"29","key":"10.1016\/j.bioorg.2022.106204_b0180","doi-asserted-by":"crossref","first-page":"8519","DOI":"10.1021\/bi9928905","article-title":"Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme","volume":"39","author":"Araujo","year":"2000","journal-title":"Biochemistry"},{"issue":"50","key":"10.1016\/j.bioorg.2022.106204_b0185","doi-asserted-by":"crossref","first-page":"15729","DOI":"10.1021\/bi048423r","article-title":"Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates","volume":"43","author":"Bersanetti","year":"2004","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0190","doi-asserted-by":"crossref","first-page":"1971","DOI":"10.1038\/nprot.2006.306","article-title":"A continuous fluorescence resonance energy transfer angiotensin I-converting enzyme assay","volume":"1","author":"Carmona","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bioorg.2022.106204_b0195","unstructured":"R. Chang, Physical Chemistry for the Biosciences, first ed., University Science Books, Sausalito, CA, 2005 - Chapter 10."},{"issue":"6","key":"10.1016\/j.bioorg.2022.106204_b0200","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1111\/febs.13647","article-title":"Kinetic and structural characterization of amyloid-\u03b2 peptide hydrolysis by human angiotensin-1-converting enzyme","volume":"283","author":"Larmuth","year":"2016","journal-title":"FEBS J."},{"key":"10.1016\/j.bioorg.2022.106204_b0205","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/srep00717","article-title":"Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides","volume":"2","author":"Masuyer","year":"2012","journal-title":"Sci. Rep."},{"issue":"16","key":"10.1016\/j.bioorg.2022.106204_b0210","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1002\/jcc.20290","article-title":"The Amber biomolecular simulation programs","volume":"26","author":"Case","year":"2005","journal-title":"J. Comput. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2022.106204_b0215","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.jctc.5b00255","article-title":"ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB","volume":"11","author":"Maier","year":"2015","journal-title":"J. Chem. Theory Comput."},{"issue":"30","key":"10.1016\/j.bioorg.2022.106204_b0220","doi-asserted-by":"crossref","first-page":"8753","DOI":"10.1021\/bi700253q","article-title":"Simulated interactions between angiotensin-converting enzyme and substrate gonadotropin-releasing hormone: novel insights into domain selectivity","volume":"46","author":"Papakyriakou","year":"2007","journal-title":"Biochemistry"},{"issue":"9","key":"10.1016\/j.bioorg.2022.106204_b0225","doi-asserted-by":"crossref","first-page":"3878","DOI":"10.1021\/ct400314y","article-title":"Routine microsecond molecular dynamics simulations with AMBER on GPUs. 2. Explicit solvent particle mesh Ewald","volume":"9","author":"Salomon-Ferrer","year":"2013","journal-title":"J. Chem. Theory Comput."},{"issue":"7","key":"10.1016\/j.bioorg.2022.106204_b0230","doi-asserted-by":"crossref","first-page":"3084","DOI":"10.1021\/ct400341p","article-title":"PTRAJ and CPPTRAJ: software for processing and analysis of molecular dynamics trajectory data","volume":"9","author":"Roe","year":"2013","journal-title":"J. Chem. Theory Comput."},{"issue":"12","key":"10.1016\/j.bioorg.2022.106204_b0235","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1021\/ar000033j","article-title":"Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models","volume":"33","author":"Kollman","year":"2000","journal-title":"Acc. Chem. Res."},{"issue":"5","key":"10.1016\/j.bioorg.2022.106204_b0240","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1517\/17460441.2015.1032936","article-title":"The MM\/PBSA and MM\/GBSA methods to estimate ligand-binding affinities","volume":"10","author":"Genheden","year":"2015","journal-title":"Expert Opin. Drug Discov."},{"issue":"27","key":"10.1016\/j.bioorg.2022.106204_b0245","doi-asserted-by":"crossref","first-page":"2436","DOI":"10.1002\/jcc.24467","article-title":"Calculating protein-ligand binding affinities with MMPBSA: method and error analysis","volume":"37","author":"Wang","year":"2016","journal-title":"J. Comput. Chem."},{"issue":"29","key":"10.1016\/j.bioorg.2022.106204_b0250","doi-asserted-by":"crossref","first-page":"3583","DOI":"10.2174\/092986706779026165","article-title":"Towards predictive ligand design with free-energy based computational methods?","volume":"13","author":"Foloppe","year":"2006","journal-title":"Curr. Med. Chem."},{"issue":"6","key":"10.1016\/j.bioorg.2022.106204_b0255","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.1002\/prot.23018","article-title":"Virtual screening using molecular simulations","volume":"79","author":"Yang","year":"2011","journal-title":"Proteins"},{"key":"10.1016\/j.bioorg.2022.106204_b0260","doi-asserted-by":"crossref","first-page":"87","DOI":"10.3389\/fmolb.2017.00087","article-title":"Recent developments and applications of the MMPBSA method","volume":"4","author":"Wang","year":"2017","journal-title":"Front. Mol. Biosci."},{"issue":"42","key":"10.1016\/j.bioorg.2022.106204_b0265","doi-asserted-by":"crossref","first-page":"12263","DOI":"10.1021\/jp073399n","article-title":"Implicit nonpolar solvent models","volume":"111","author":"Tan","year":"2007","journal-title":"J. Phys. Chem. B."},{"issue":"4612","key":"10.1016\/j.bioorg.2022.106204_b0270","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1126\/science.6879170","article-title":"Solvent-accessible surfaces of proteins and nucleic acids","volume":"221","author":"Connolly","year":"1983","journal-title":"Science"},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0275","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1002\/(SICI)1096-987X(19990130)20:2<217::AID-JCC4>3.0.CO;2-A","article-title":"Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)","volume":"20","author":"Weiser","year":"1999","journal-title":"J. Comput. Chem."},{"issue":"37","key":"10.1016\/j.bioorg.2022.106204_b0280","doi-asserted-by":"crossref","first-page":"18680","DOI":"10.1021\/jp063479b","article-title":"How well does Poisson-Boltzmann implicit solvent agree with explicit solvent? A quantitative analysis","volume":"110","author":"Tan","year":"2006","journal-title":"J. Phys. Chem. B"},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0285","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1002\/1097-0282(2000)56:4<275::AID-BIP10024>3.0.CO;2-E","article-title":"Theory and applications of the Generalized Born solvation model in macromolecular simulations","volume":"56","author":"Tsui","year":"2000","journal-title":"Biopolymers"},{"issue":"8","key":"10.1016\/j.bioorg.2022.106204_b0290","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1007\/BF01930447","article-title":"Inhibition of angiotensin-converting enzyme by analogs of peptides from Bothrops jararaca venom","volume":"29","author":"Cushman","year":"1973","journal-title":"Experientia"},{"issue":"19","key":"10.1016\/j.bioorg.2022.106204_b0295","doi-asserted-by":"crossref","first-page":"6065","DOI":"10.1021\/bi012121x","article-title":"Selective inhibition of the C-domain of angiotensin I converting enzyme by bradykinin potentiating peptides","volume":"41","author":"Cotton","year":"2002","journal-title":"Biochemistry"},{"issue":"8","key":"10.1016\/j.bioorg.2022.106204_b0300","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1111\/j.1742-4658.2006.05196.x","article-title":"Combined use of selective inhibitors and fluorogenic substrates to study the specificity of somatic wild-type angiotensin-converting enzyme","volume":"273","author":"Jullien","year":"2006","journal-title":"FEBS J."},{"issue":"1","key":"10.1016\/j.bioorg.2022.106204_b0305","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1042\/BJ20100056","article-title":"Characterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinopril","volume":"428","author":"Watermeyer","year":"2010","journal-title":"Biochem. J."},{"issue":"24","key":"10.1016\/j.bioorg.2022.106204_b0310","doi-asserted-by":"crossref","first-page":"9826","DOI":"10.1021\/jm4009345","article-title":"N- Versus C-Domain selectivity of catalytic inactivation of human angiotensin converting enzyme by lisinopril-coupled transition metal chelates","volume":"56","author":"Hocharoen","year":"2013","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0315","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1073\/pnas.82.4.1025","article-title":"Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone","volume":"82","author":"Skidgel","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0320","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0026-895X(25)14945-6","article-title":"Carboxyl-terminal tripeptidyl hydrolysis of substance P by purified rabbit lung angiotensin-converting enzyme and the potentiation of substance P activity in vivo by captopril and MK-422","volume":"25","author":"Cascieri","year":"1984","journal-title":"Mol. Pharmacol."},{"issue":"4","key":"10.1016\/j.bioorg.2022.106204_b0325","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0196-9781(99)00031-5","article-title":"Potentiation of the hypotensive effect of bradykinin by angiotensin-(1\u20137)-related peptides","volume":"20","author":"Paula","year":"1999","journal-title":"Peptides"},{"issue":"1","key":"10.1016\/j.bioorg.2022.106204_b0330","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1042\/BJ20040634","article-title":"Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism","volume":"383","author":"Rice","year":"2004","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.bioorg.2022.106204_b0335","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1161\/HYPERTENSIONAHA.111.180844","article-title":"Increased angiotensin II-induced hypertension and inflammatory cytokines in mice lacking angiotensin-converting enzyme N domain activity","volume":"59","author":"Ong","year":"2012","journal-title":"Hypertension"}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206822006101?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206822006101?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T08:47:23Z","timestamp":1758617243000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206822006101"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12]]},"references-count":67,"alternative-id":["S0045206822006101"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2022.106204","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2022,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Peptide inhibitors of angiotensin-I converting enzyme based on angiotensin (1\u20137) with selectivity for the C-terminal domain","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2022.106204","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"106204"}}